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3ZHW

X-ray Crystallographic Structural Characteristics of Arabidopsis Hemoglobin I and their Functional Implications

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0005344molecular_functionoxygen carrier activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0009505cellular_componentplant-type cell wall
A0009506cellular_componentplasmodesma
A0016491molecular_functionoxidoreductase activity
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0071456biological_processcellular response to hypoxia
B0001666biological_processresponse to hypoxia
B0005344molecular_functionoxygen carrier activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0009505cellular_componentplant-type cell wall
B0009506cellular_componentplasmodesma
B0016491molecular_functionoxidoreductase activity
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0071456biological_processcellular response to hypoxia
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 1163
ChainResidue
ALYS65
APHE114
AALA117
ALEU148
AHOH2022
AHOH2045
AHOH2071
BLEU158
BASN160
AHIS69
ASER72
AARG99
ALEU100
ASER103
AHIS104
ATYR107
AHIS113

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1902
ChainResidue
ALYS126
ATRP133
ALYS138
AHOH2049

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1904
ChainResidue
ALYS118
AVAL139
AGLY142
AGLN143
AASP146

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1905
ChainResidue
ALEU53
AARG54
ALYS65

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM B 1163
ChainResidue
BPHE50
BLYS65
BHIS69
BARG99
BLEU100
BSER103
BHIS104
BTYR107
BHIS113
BPHE114
BALA117
BVAL149

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1906
ChainResidue
BLYS126
BTRP133
BLYS138
BHOH2046
BHOH2056

Functional Information from PROSITE/UniProt
site_idPS00208
Number of Residues12
DetailsPLANT_GLOBIN Plant hemoglobins signature. NPkLkpHAmsvF
ChainResidueDetails
AASN63-PHE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68168
ChainResidueDetails
ASER51
BSER51

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23485912, ECO:0007744|PDB:3ZHW
ChainResidueDetails
ALYS65
AARG99
BLYS65
BARG99

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:23485912, ECO:0007744|PDB:3ZHW
ChainResidueDetails
AHIS69
BHIS69

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O04986
ChainResidueDetails
ASER103
BSER103

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:23485912, ECO:0007744|PDB:3ZHW
ChainResidueDetails
AHIS104
BHIS104

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Homodimerization => ECO:0000269|PubMed:23485912, ECO:0007744|PDB:3ZHW
ChainResidueDetails
ALYS138
BLYS138

224004

PDB entries from 2024-08-21

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